ID A0A7D7KRH9_9MAGN Unreviewed; 393 AA. AC A0A7D7KRH9; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 29-SEP-2021, entry version 4. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01358}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358}; DE AltName: Full=NAD(P)H dehydrogenase, subunit H {ECO:0000256|HAMAP-Rule:MF_01358}; DE AltName: Full=NADH-plastoquinone oxidoreductase 49 kDa subunit {ECO:0000256|HAMAP-Rule:MF_01358}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit H {ECO:0000256|HAMAP-Rule:MF_01358}; GN Name=ndhH {ECO:0000256|HAMAP-Rule:MF_01358, GN ECO:0000313|EMBL:QMS49548.1}; OS Actinodaphne obovata. OG Plastid; Chloroplast {ECO:0000313|EMBL:QMS49548.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; OC Actinodaphne. OX NCBI_TaxID=155287 {ECO:0000313|EMBL:QMS49548.1}; RN [1] {ECO:0000313|EMBL:QMS49548.1} RP NUCLEOTIDE SEQUENCE. RA Xiao T.; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain CC and possibly in a chloroplast respiratory chain. The immediate electron CC acceptor for the enzyme in this species is believed to be CC plastoquinone. Couples the redox reaction to proton translocation, and CC thus conserves the redox energy in a proton gradient. CC {ECO:0000256|HAMAP-Rule:MF_01358}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561, CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01358}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561, CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01358}; CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. {ECO:0000256|HAMAP-Rule:MF_01358}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01358}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01358}; Stromal side {ECO:0000256|HAMAP- CC Rule:MF_01358}. CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family. CC {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358, CC ECO:0000256|RuleBase:RU003685}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MN274947; QMS49548.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.645.10; -; 1. DR HAMAP; MF_01358; NDH1_NuoD; 1. DR InterPro; IPR001135; NADH_Q_OxRdtase_suD. DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS. DR InterPro; IPR022885; NDH1_su_D/H. DR InterPro; IPR029014; NiFe-Hase_large. DR Pfam; PF00346; Complex1_49kDa; 1. DR SUPFAM; SSF56762; SSF56762; 1. DR PROSITE; PS00535; COMPLEX1_49K; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:QMS49548.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01358}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01358}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01358}; KW Plastid {ECO:0000313|EMBL:QMS49548.1}; KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01358}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01358}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01358}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_01358}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01358}. FT DOMAIN 124..393 FT /note="Complex1_49kDa" FT /evidence="ECO:0000259|Pfam:PF00346" SQ SEQUENCE 393 AA; 45315 MW; 97EF38A2EB761468 CRC64; MNVPATRKGL MIVNMGPHHP SMHGVLRLIV TLDGEDVIDC EPVLGYLHRG MEKIAENRTI IQYLPYVTRW DYLATMFTEA ITVNAPEQLG NIQVPKRASY IRVIMLELSR IASHLLWLGP FMADIGSQTP FFYIFREREL LYDLFEAATG MRMMHNYFRI GGVAADLPHG WIDKCLDFCD YSLTGIVEYQ KLITQNPIFL ERVEGVGIIG GEEAINWGLS GPMLRASGIQ WDLRKVDHYE CYDEFDWEVQ WQKEGDSLAR YLVRINEMKE SIKIIQQALE GIPGGPYENL EVRRFDRASD SEWNGFEYRF ISKKPSPTFE LSKQELYVRV EAPKGELGIF LIGDNSVFPW RWKIRPPGFI NLQILPQLIK RMKLADIMTI LGSIDIIMGE VDR //